A role for alpha- and beta-catenins in bacterial uptake

Citation
M. Lecuit et al., A role for alpha- and beta-catenins in bacterial uptake, P NAS US, 97(18), 2000, pp. 10008-10013
Citations number
37
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN journal
00278424 → ACNP
Volume
97
Issue
18
Year of publication
2000
Pages
10008 - 10013
Database
ISI
SICI code
0027-8424(20000829)97:18<10008:ARFAAB>2.0.ZU;2-J
Abstract
Interaction of internalin with E-cadherin promotes entry of Listeria monocy togenes into human epithelial cells. This process requires actin cytoskelet on rearrangements. Here we show, by using a series of stably transfected ce ll lines expressing E-cadherin variants, that the ectodomain of E-cadherin is sufficient for bacterial adherence and that the intracytoplasmic domain is required for entry. The critical cytoplasmic region was further mapped t o the beta-catenin binding domain. Because beta-catenin is known to interac t with alpha-catenin, which binds to actin, we generated a fusion molecule consisting of the ectodomain of E-cadherin and the actin binding site of al pha-catenin. Cells expressing this chimera were as permissive as E-cadherin -expressing cells. In agreement with these data, alpha- and beta-catenins a s well as E-cadherin clustered and colocalized at the entry site, where F-a ctin then accumulated. Taken together, these results reveal that E-cadherin , via beta- and alpha-catenins, can trigger dynamic events of actin polymer ization and membrane extensions culminating in bacterial uptake.